| Home > Research literature > Bachelor's degree final project > An in silico analysis of laccase thermostability determinants for the improvement of rational enzyme engineering |
| Date: | 2026 |
| Abstract: | Laccases (EC:1. 10. 3. 2) are enzymes of the multi-copper oxidase family capable of degrading a wide range of substrates using oxygen as the final electron acceptor and producing water as a by-product of the reaction. Owing to this characteristic, they are promising tools in the field of bioremediation. However, the application of laccases in large-scale procedures is hindered by the low thermostability of many of these enzymes, a property whose molecular determinants remain to be fully characterised. Therefore, the aim of this project was to analyse thermostable and non-thermostable laccases to elucidate their physicochemical differences and identify key residues contributing to thermostability. To achieve this, multiple-sequence alignments of thermostable and non-thermostable laccases were constructed and analysed through statistical tests and the Kullback-Leibler divergence. The analysis revealed a high degree of global similarity between the two groups of enzymes, suggesting that thermostability is mostly determined by local conservation patterns. Using the Kullback-Leibler divergence and Bacillus subtilis CotA structure as a reference, several discriminating positions were identified and structurally interpreted, revealing conservation patterns with a potential to be used in the targeted rational design of laccases to increase their thermostability. |
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| Language: | Anglès |
| Studies: | Microbiologia [3602] |
| Study plan: | Grau en Microbiologia [816] |
| Document: | Treball final de grau |
| Subject: | Bacterial laccase ; Thermostability ; Bioremediation ; Rational engineering ; Multiple-sequence alignment (MSA) |
Pòster 1 p, 4.7 MB |
TFG 24 p, 7.3 MB |